Role of Acidic Amino Acid Residues of PsaD Subunit on Limiting the Affinity of Photosystem I for Ferredoxin

2001 ◽  
Vol 287 (4) ◽  
pp. 833-836 ◽  
Author(s):  
Hervé Bottin ◽  
Jonathan Hanley ◽  
Bernard Lagoutte
Keyword(s):  
Amino Acid ◽  
Photosystem I ◽  
Amino Acid Residues ◽  
Acidic Amino Acid

scholarly journals Role of Integrase in Reverse Transcription of the Saccharomyces cerevisiae Retrotransposon Ty1

2005 ◽  
Vol 4 (6) ◽  
pp. 1057-1065 ◽  
Author(s):  
M. Wilhelm ◽  
F.-X. Wilhelm
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Amino Acid ◽  
Specific Activity ◽  
Rnase H ◽  
Amino Acid Residues ◽  
Acidic Amino Acid ◽  
Acidic Domain ◽  
Basic Region

ABSTRACT Reverse transcriptase (RT) with its associated RNase H (RH) domain and integrase (IN) are key enzymes encoded by retroviruses and retrotransposons. Several studies have implied a functional role of the interaction between IN and RT during the replication of retroviral and retrotransposon genomes. In this study, IN deletion mutants were used to investigate the role of IN on the RT activity of the yeast Saccharomyces cerevisiae retrotransposon Ty1. We have identified two domains of Ty1 integrase which have effects on RT activity in vivo. The deletion of a domain spanning amino acid residues 233 to 520 of IN increases the exogenous specific activity of RT up to 20-fold, whereas the removal of a region rich in acidic amino acid residues between residues 521 and 607 decreases its activity. The last result complements our observation that an active recombinant RT protein can be obtained if a small acidic tail mimicking the acidic domain of IN is fused to the RT-RH domain. We suggest that interaction between these acidic amino acid residues of IN and a basic region of RT could be critical for the correct folding of RT and for the formation of an active conformation of the enzyme.

scholarly journals Local stability identification and the role of key acidic amino acid residues in staphylococcal nuclease unfolding

FEBS Journal ◽  
2005 ◽  
Vol 272 (15) ◽  
pp. 3967-3974 ◽  
Author(s):  
Hueih-Min Chen ◽  
Siu-Chiu Chan ◽  
King-Wong Leung ◽  
Jiun-Ming Wu ◽  
Huey-Jen Fang ◽  
...  
Keyword(s):  
Amino Acid ◽  
Local Stability ◽  
Staphylococcal Nuclease ◽  
Amino Acid Residues ◽  
Acidic Amino Acid

The Role of Acidic Amino Acid Residues in the Structural Stability of Snake Cardiotoxins†

Biochemistry ◽  
1996 ◽  
Vol 35 (28) ◽  
pp. 9177-9186 ◽  
Author(s):  
Chien-Min Chiang ◽  
Shou-Lin Chang ◽  
Hai-jui Lin ◽  
Wen-guey Wu
Keyword(s):  
Amino Acid ◽  
Structural Stability ◽  
Amino Acid Residues ◽  
Acidic Amino Acid

Role of acidic amino acid residues in chitooligosaccharide-binding to Streptomyces sp. N174 chitosanase

2005 ◽  
Vol 338 (4) ◽  
pp. 1839-1844 ◽  
Author(s):  
Tomomi Katsumi ◽  
Marie-Ève Lacombe-Harvey ◽  
Hugo Tremblay ◽  
Ryszard Brzezinski ◽  
Tamo Fukamizo
Keyword(s):  
Amino Acid ◽  
Amino Acid Residues ◽  
Acidic Amino Acid ◽  
Streptomyces Sp

scholarly journals Role of lysine and acidic amino acid residues on the insecticidal activity of Jackbean urease

Toxicon ◽  
2013 ◽  
Vol 71 ◽  
pp. 76-83 ◽  
Author(s):  
Rafael Real-Guerra ◽  
Célia Regina Carlini ◽  
Fernanda Stanisçuaski
Keyword(s):  
Amino Acid ◽  
Insecticidal Activity ◽  
Amino Acid Residues ◽  
Acidic Amino Acid

scholarly journals Deletion of the Actin-Associated Tropomyosin Tpm3 Leads to Reduced Cell Complexity in Cultured Hippocampal Neurons—New Insights into the Role of the C-Terminal Region of Tpm3.1

Cells ◽  
2021 ◽  
Vol 10 (3) ◽  
pp. 715
Author(s):  
Tamara Tomanić ◽  
Claire Martin ◽  
Holly Stefen ◽  
Esmeralda Parić ◽  
Peter Gunning ◽  
...  
Keyword(s):  
Amino Acid ◽  
Hippocampal Neurons ◽  
Molecular Mechanisms ◽  
Growth Cones ◽  
Amino Acid Residues ◽  
Terminal Amino Acid ◽  
C Terminus ◽  
Primary Mouse ◽  
Terminal Amino

Tropomyosins (Tpms) have been described as master regulators of actin, with Tpm3 products shown to be involved in early developmental processes, and the Tpm3 isoform Tpm3.1 controlling changes in the size of neuronal growth cones and neurite growth. Here, we used primary mouse hippocampal neurons of C57/Bl6 wild type and Bl6Tpm3flox transgenic mice to carry out morphometric analyses in response to the absence of Tpm3 products, as well as to investigate the effect of C-terminal truncation on the ability of Tpm3.1 to modulate neuronal morphogenesis. We found that the knock-out of Tpm3 leads to decreased neurite length and complexity, and that the deletion of two amino acid residues at the C-terminus of Tpm3.1 leads to more detrimental changes in neurite morphology than the deletion of six amino acid residues. We also found that Tpm3.1 that lacks the 6 C-terminal amino acid residues does not associate with stress fibres, does not segregate to the tips of neurites, and does not impact the amount of the filamentous actin pool at the axonal growth cones, as opposed to Tpm3.1, which lacks the two C-terminal amino acid residues. Our study provides further insight into the role of both Tpm3 products and the C-terminus of Tpm3.1, and it forms the basis for future studies that aim to identify the molecular mechanisms underlying Tpm3.1 targeting to different subcellular compartments.

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